کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
443239 | 692692 | 2016 | 7 صفحه PDF | دانلود رایگان |
• Hydrophobin HFBII is stable in water and in fluorinated emulsions.
• Atomistic simulations of HFBII in water/oil support the observed stability.
• Circular dichroism in water/oil emulsion show the structural stability of HFBII.
• Computer simulations predict HFBII migration at the water/air interface.
Hydrophobins are proteins of interest for numerous applications thanks to their unique conformational and surface properties and their ability to self-assemble at interfaces. Here we report fully atomistic molecular mechanics and molecular dynamics results together with circular dichroism experimental data, aimed to study the conformational properties of the hydrophobin HFBII in a fluorinated solvent in comparison with a water solution and/or at an aqueous/vacuum interface. Both the atomistic simulations and the circular dichroism data show the remarkable structural stability of HFBII at all scales in all these environments, with no significant structural change, although a small cavity is formed in the fluorinated solvent. The combination of theoretical calculations and circular dichroism data can describe in detail the protein conformation and flexibility in different solvents and/or at an interface, and constitutes a first step towards the study of their self-assembly.
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Journal: Journal of Molecular Graphics and Modelling - Volume 63, January 2016, Pages 8–14